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Conformational characteristics of peptides containing α,β‐dehydroamino acid residues
Author(s) -
Jain Ratanmani,
Chauhan Virander S.
Publication year - 1996
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1996)40:1<105::aid-bip5>3.0.co;2-#
Subject(s) - chemistry , peptide , residue (chemistry) , delta , stereochemistry , turn (biochemistry) , amino acid residue , crystallography , cyclic peptide , crystal structure , peptide sequence , biochemistry , engineering , gene , aerospace engineering
The structural preferences of synthetic peptides containing α,β‐dehydroamino acid residues, as determined by theoretical studies, x‐ray diffraction analyses, and spectroscopic studies, are reviewed. The role of Δ Z Phe residues in stabilizing type II β‐turn structures in small peptides and in nucleating helical structure in longer peptides is exemplified by several crystal as well as solution structural studies. From the few studies reported so far it appears that Δ Z Leu influences the peptide backbone, much like the Δ Z Phe residue, whereas ΔAla prefers the extended conformation, suggesting that the nature of β substituents might influence the conformation restriction behavior of the dehydroresidues. Conformational studies on synthetic peptides containing Δ E , Δ Z Abu, and ΔVal have also been described. © 1996 John Wiley & Sons, Inc.